Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Panretinal photocoagulation (PRP) reduces the incidence of severe visual loss in proliferative diabetic retinopathy (PDR). The aim of the study was to determine the effect of PRP on the activity of matrix metalloproteinase-2 (MMP-2) and MMP-9, and also on the alpha(2)-Macroglobulin (alpha(2)M) proteolytic state in the vitreous of eyes with PDR. Vitreous samples were obtained from patients undergoing vitrectomy for the treatment of retinal diseases: 17 with PDR and eight with idiopathic macular hole (MH). Qualitative evaluation of the MMP-2 and MMP-9 activation status was performed by gelatin zymography and quantitative assay was carried out for vitreous total protein content and alpha(2)M. The proteolytic state of alpha(2)M was evaluated by Western blotting. Although all vitreous samples contained proMMP-2, increased proMMP-9 and active MMP-9 were detected in PDR samples without PRP. In addition, after PRP the proMMP-9 activity was significantly decreased, whereas the proMMP-2 activity was not affected. Enhanced total protein and alpha(2)M concentrations were observed in all vitreous samples from PDR patients with and without previous PRP compared with samples from patients with MH. However, a differential proteolytic state of alpha(2)M, expressed as 180/85-90kDa ratio, was detected among PDR patients with and without PRP treatment. Whereas a low 180/85-90kDa ratio of alpha(2)M in vitreous of PDR patients without PRP was observed, a high proportion of 180kDa subunit was principally detected in PDR with PRP. These results demonstrate that PDR occurs with an enhanced activity of MMP-9 and activation of alpha(2)M by proteinases, which is reversed after PRP. In addition, we suggest that alpha(2)M plays a key role in the control and regulation of the ocular neovascularization involved in the pathogenesis of ischemic retinal diseases such as PDR.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.exer.2007.07.018 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Engineering of a Complex of the DNase Domain of Colicin E9 with the Immunity Protein Im9 Activated by the Protease pS273R of African Swine Fever Virus.
ACS Synth Biol
September 2025
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow 119071, Russian Federation.
African swine fever virus (ASFV) is a large DNA virus that causes a highly lethal disease in pigs and currently has no effective vaccines or antiviral treatments available. We designed a protein switch that combines the DNase domain of colicin E9 (DNase E9) and its inhibitor Im9 with the viral protease cleavage site. The complex is only destroyed in the presence of an ASFV pS273R protease, which releases DNase activity.
View Article and Find Full Text PDFWarm temperature-induced autophagy mediates selective degradation of TIMING OF CAB EXPRESSION 1 thus promoting plant thermomorphogenesis.
Plant Cell
September 2025
Department of Plant Sciences, College of Biological Sciences, State Key Laboratory of Plant Environmental Resilience, China Agricultural University, Beijing 100193, China.
Plant thermomorphogenesis is a critical adaptive response to elevated ambient temperatures. The transcription factor PHYTOCHROME-INTERACTING FACTOR 4 (PIF4) integrates diverse environmental and phytohormone signals to coordinate thermoresponsive growth. However, the cellular mechanisms underlying plant thermomorphogenic growth remain poorly understood.
View Article and Find Full Text PDFCaseinolytic Protease P: A Therapeutic Nexus in Infection, Inflammation, and Immunity.
Crit Rev Immunol
September 2025
Department of Pharmacy, Birla Institute of Technology and Science (BITS) Pilani, Hyderabad Campus, Dist. Medchal,500078, Telangana State, India.
Caseinolytic protease P (ClpP) is a highly conserved serine protease that plays a pivotal role in protein homeostasis and quality control in bacteria, mitochondria of mammalian cells, and plant chloroplasts. As the proteolytic core of the ATP-dependent Clp protease complex, ClpP partners with regulatory ATPases (e.g.
View Article and Find Full Text PDFTargeted degradation of Werner syndrome helicase (WRN) via ligand-directed covalent hydrophobic tagging.
Eur J Med Chem
September 2025
State Key Laboratory of Natural Medicines and Department of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University, Nanjing, 211198, PR China. Electronic address:
The Werner syndrome RecQ helicase (WRN) has recently emerged as a novel synthetic lethality target for microsatellite instability-high (MSI-H) cancers. However, available WRN inhibitors or degraders is still lacking so far. Particularly, chemically designed probes capable of degrading WRN irrespective of microsatellite status remain unexplored.
View Article and Find Full Text PDFCobalt-Doped Carbon Quantum Dots Work Synergistically with Weak Acetic Acid to Eliminate Antimicrobial-Resistant Bacterial Infections.
ACS Nano
September 2025
Department of Biomedicine, University of Bergen, Bergen 5009, Norway.
When pathogenic bacteria colonize a wound, they can create an alkaline ecological niche that selects for their survival by creating an inflammatory environment restricting healthy wound healing to proceed. To aid healing, wound acidification has been exploited to disrupt this process and stimulate fibroblast growth, increase wound oxygen concentrations, minimize proteolytic activity, and restimulate the host immune system. Within this study, we have developed cobalt-doped carbon quantum dot nanoparticles that work together with mild acetic acid, creating a potent synergistic antimicrobial therapy.
View Article and Find Full Text PDF